| Identification |
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| Name: | Guanylate kinase |
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| Synonyms: | |
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| Gene Name: | gmk |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in protein binding |
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| Specific Function: | Essential for recycling GMP and indirectly, cGMP |
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| Cellular Location: | Cytoplasm |
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| SMPDB Pathways: | - purine nucleotides de novo biosynthesis PW000910
- purine nucleotides de novo biosynthesis 1435709748 PW000960
- purine nucleotides de novo biosynthesis 2 PW002033
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| KEGG Pathways: | |
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| KEGG Reactions: | |
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| SMPDB Reactions: | |
1.0 | + | 1.0 | → | 1.0Adenosine diphosphate | + | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
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| Complex Reactions: | |
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| Metabolites: | |
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| GO Classification: | | Function |
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| catalytic activity | | guanylate kinase activity | | phosphotransferase activity, phosphate group as acceptor | | transferase activity | | transferase activity, transferring phosphorus-containing groups | | Process |
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| cellular nitrogen compound metabolic process | | metabolic process | | nitrogen compound metabolic process | | nucleobase, nucleoside and nucleotide metabolic process | | nucleobase, nucleoside, nucleotide and nucleic acid metabolic process | | nucleoside phosphate metabolic process | | nucleotide metabolic process | | purine nucleotide metabolic process |
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| Gene Properties |
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| Blattner: | b3648 |
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| Gene Orientation | Clockwise |
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| Centisome Percentage: | 82.32 |
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| Left Sequence End | 3819451 |
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| Right Sequence End | 3820074 |
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| Gene Sequence: | >624 bp
ATGTCAGGTCTGCCACAGGGCAGACCAACGTTTGGCGCTGCGCAAAACGTGAGCGCGGTG
GTGGCGTATGACTTATCTGCCCACATGCTGGATGTCGTGGCACAAGCTGCCGAAGCCCGG
CAACTGAAAAATATCACCACCCGCCAGGGATATGCCGAAAGTCTGCCATTTGCCGATAAC
GCATTTGATATTGTTATCAGCCGTTATTCTGCCCATCACTGGCATGATGTTGGTGCAGCA
CTGCGAGAAGTGAATAGGATATTGAAACCTGGCGGTAGGCTGATTGTGATGGACGTAATG
TCTCCGGGTCACCCAGTGCGCGACATCTGGTTACAGACGGTAGAAGCATTACGCGATACC
TCTCACGTACGAAACTACGCCAGCGGTGAGTGGTTGACGTTAATCAATGAAGCCAATCTG
ATAGTTGATAATTTAATTACAGATAAGTTACCGCTGGAATTTTCTTCATGGGTCGCGAGA
ATGCGTACGCCAGAAGCGTTAGTAGACGCTATTCGCATTTACCAACAGAGCGCATCGACA
GAGGTGAGAACGTATTTTGCCTTGCAGAATGATGGCTTTTTCACCAGTGATATCATCATG
GTAGATGCACATAAAGCGGCATAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 207 |
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| Protein Molecular Weight: | 23593 |
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| Protein Theoretical pI: | 7 |
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| PDB File: | 1S96 |
| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Guanylate kinase
MAQGTLYIVSAPSGAGKSSLIQALLKTQPLYDTQVSVSHTTRQPRPGEVHGEHYFFVNHD
EFKEMISRDAFLEHAEVFGNYYGTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARS
IFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDYLIVNDDFDTALTDLK
TIIRAERLRMSRQKQRHDALISKLLAD |
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| References |
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| External Links: | |
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| General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
- Gentry, D., Bengra, C., Ikehara, K., Cashel, M. (1993). "Guanylate kinase of Escherichia coli K-12." J Biol Chem 268:14316-14321. Pubmed: 8390989
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
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